BCL-2 proteins and apoptosis: Recent insights and unknowns
- Institute for Biochemistry and Molecular Biology, University of Freiburg, Stefan-Meier-Str.17, 79104 Freiburg (Germany)
Highlights: • The pro-apoptotic BCL-2 proteins can commit cells to apoptosis. • BAX and BAK are regulated by dynamic shuttling between mitochondria and cytosol of healthy cells. • BH3-only proteins, regulators of BAX and BAK, are not required for BAX activation. • Recent super-resolution microscopy studies provide novel insights into the active BAX complex. Proteins of the B-cell lymphoma-2 (BCL-2) family control the intrinsic apoptosis pathway. The pro-apoptotic BCL-2 proteins BAX and BAK can commit a cell to its programmed death by permeabilizing the outer mitochondrial membrane (OMM) and subsequent initiation of the caspase cascade. Therefore, the activities of BAX and BAK are precisely controlled by a complex network of proteins inside and outside the BCL-2 family. Cells survive by constant control of dynamic translocation and retrotranslocation of BAX and BAK to the mitochondria and back into the cytosol. Recent insights into BAX/BAK shuttling, BCL-2 protein interactions, the role of BH3-only proteins in apoptosis signaling and the active BAX complex set the stage for the development of novel strategies in cancer therapy and the analysis of cellular predisposition to apoptosis.
- OSTI ID:
- 23125228
- Journal Information:
- Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 1 Vol. 500; ISSN 0006-291X; ISSN BBRCA9
- Country of Publication:
- United States
- Language:
- English
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